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• W3031201813 abstract "Abstract The Siah1 and Siah2 ubiquitin ligases are implicated in diverse biological processes ranging from cellular stress responses, signaling to transcriptional regulation. A key substrate of Siah1 is ELL2, which undergoes proteolysis upon polyubiquitination. ELL2 stimulates transcriptional elongation and is a subunit of the Super Elongation Complex (SEC) essential for HIV-1 transactivation. Previously, multiple transcriptional and post-translational mechanisms are reported to control Siah's expression and activity. Here we show that the activity of Siah1/2 can also be suppressed by host cell factor 1 (HCF1), and the hitherto poorly characterized HCF2, which themselves are not degraded but can bind and block the substrate-binding domain (SBD) of Siah1/2 to prevent their autoubiquitination and trans-ubiquitination of downstream targets including ELL2. This effect stabilizes ELL2 and enhances the ELL2-SEC formation for robust HIV-1 transactivation. Thus, our study not only identifies HCF1/2 as novel activators of HIV-1 transcription through inhibiting Siah1 to stabilize ELL2, but also reveals the SBD of Siah1/2 as a previously unrecognized new target for HCF1/2 to exert this inhibition." @default.
• W3031201813 created "2020-06-05" @default.
• W3031201813 creator A5015348295 @default.
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• W3031201813 creator A5049838965 @default.
• W3031201813 date "2020-06-01" @default.
• W3031201813 modified "2023-09-24" @default.
• W3031201813 title "Host cell factors stimulate HIV-1 transcription by antagonizing substrate-binding function of Siah1 ubiquitin ligase to stabilize transcription elongation factor ELL2" @default.
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• W3031201813 doi "https://doi.org/10.1093/nar/gkaa461" @default.
• W3031201813 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7367184" @default.
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• W3031201813 hasPublicationYear "2020" @default.
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